ID   ENV_HAPV1               Reviewed;         518 AA.
AC   C1JJY3;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   02-DEC-2020, entry version 32.
DE   RecName: Full=Envelope protein;
DE            Short=Env;
DE   AltName: Full=Virion protein 4;
DE            Short=VP4;
DE   Flags: Precursor;
GN   ORFNames=ORF4;
OS   Halorubrum pleomorphic virus 1 (HRPV-1).
OC   Viruses; Monodnaviria; Trapavirae; Saleviricota; Huolimaviricetes;
OC   Haloruvirales; Pleolipoviridae; Alphapleolipovirus;
OC   Alphapleolipovirus HRPV1.
OX   NCBI_TaxID=634168;
OH   NCBI_TaxID=634157; Halorubrum sp. PV6.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 32-41.
RX   PubMed=19298373; DOI=10.1111/j.1365-2958.2009.06642.x;
RA   Pietila M.K., Roine E., Paulin L., Kalkkinen N., Bamford D.H.;
RT   "An ssDNA virus infecting archaea: a new lineage of viruses with a membrane
RT   envelope.";
RL   Mol. Microbiol. 72:307-319(2009).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19864380; DOI=10.1128/jvi.01347-09;
RA   Pietila M.K., Laurinavicius S., Sund J., Roine E., Bamford D.H.;
RT   "The single-stranded DNA genome of novel archaeal virus halorubrum
RT   pleomorphic virus 1 is enclosed in the envelope decorated with glycoprotein
RT   spikes.";
RL   J. Virol. 84:788-798(2010).
RN   [3]
RP   GLYCOSYLATION AT ASN-213, AND PROTEIN SEQUENCE OF 202-218.
RX   PubMed=22435790; DOI=10.1111/j.1365-2958.2012.08045.x;
RA   Kandiba L., Aitio O., Helin J., Guan Z., Permi P., Bamford D.H.,
RA   Eichler J., Roine E.;
RT   "Diversity in prokaryotic glycosylation: an archaeal-derived N-linked
RT   glycan contains legionaminic acid.";
RL   Mol. Microbiol. 84:578-593(2012).
CC   -!- FUNCTION: Envelope protein that may play a role in host-cell attachment
CC       and viral genome entry.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:19864380};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:19864380}.
CC   -!- PTM: N-glycosylated by a pentasaccharide comprising glucose, glucuronic
CC       acid and a terminal 5-N-formyl-legionaminic acid residue.
CC       {ECO:0000269|PubMed:22435790}.
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DR   EMBL; FJ685651; ACO54899.1; -; Genomic_DNA.
DR   RefSeq; YP_002791889.1; NC_012558.1.
DR   SMR; C1JJY3; -.
DR   iPTMnet; C1JJY3; -.
DR   GeneID; 7755264; -.
DR   KEGG; vg:7755264; -.
DR   Proteomes; UP000009401; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix; Virion.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000269|PubMed:19298373"
FT   CHAIN           32..518
FT                   /note="Envelope protein"
FT                   /id="PRO_5000456197"
FT   TOPO_DOM        32..485
FT                   /note="Extracellular"
FT   TRANSMEM        486..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        507..518
FT                   /note="Cytoplasmic"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT                   /evidence="ECO:0000269|PubMed:22435790"
SQ   SEQUENCE   518 AA;  56390 MW;  DA35EC9F745F2B54 CRC64;
     MSVNRSSIKS LLMVFMIVSS SLLAPVGGAA ADEFRTPAAS DTSPEAGECS NLDDFIMFLS
     VGRINADSCS RQAYVDAAVQ DMKDSDANQT KVDIYSAAAG VKGGSETWAA PYDNYLNDTE
     SIAWMKAESA IAQSYSEGES KTEAKVAAKA AIADYYATKQ KNLIEQWNFA NAQMFTLREQ
     ARMEDGISRN YVEPAYRNVE KTNSPDYSLA YSNTTVEKSL VDGTTVNTTG VSMDVTVQHT
     TVSDVATVSS GPVRAGKYNN QYNEWKATYY SWSVEPASPS QDTLYAVHFQ PYADRWQRIV
     DMNGALQSEA DNFVNATWDD YDTGQINASD VLSANTAMSE YGVRSGSESE GLWRSTAALS
     MMGYDTPNLN NSGMMTVEYK NVQHTGLLMA KNAPNGSWQV NTTYNTSNID GPVFMATTEG
     TKLDFADGEE FTIVGMTAKD GTAVNSTQTT KYRYKTANTT ELLEVQNQLI ELRQEIEDRE
     PEAGGFFGSG STDTMLVGLL ALAGVLLLAQ SNNRGGRR